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Adenosine deaminase acting on RNA refers to a family of evolutionarily conserved enzymes known as ADARs that catalyze the conversion of adenosine to inosine within double-stranded regions of cellular RNAs—a process called A-to-I editing. This modification alters base-pairing properties and can recode protein-coding sequences or affect noncoding regulatory elements. In humans there are three main isoforms—ADAR1 (with p110 constitutive and p150 interferon-inducible forms), ADAR2 (constitutively expressed), and catalytically inactive ADAR3—each with distinct tissue distributions and substrate preferences. These enzymes play critical roles across diverse biological processes including nervous system development/functionality, hematopoiesis, innate immunity discrimination between self/non-self nucleic acids via MDA5 pathway modulation, apoptosis regulation through mRNA splicing/translation changes, viral persistence control via viral genome editing/mutation rates modulation—and more recently have been implicated as promising therapeutic targets for cancer immunotherapy as well as genetic/neurodevelopmental/cardiovascular disorders when dysregulated[1][3][4][5].
Drugs or interventions targeting this molecule would typically act by inhibiting or enhancing its enzymatic activity—specifically the conversion of adenosine to inosine in double-stranded RNAs—or modulating its interaction with other proteins involved in immune signaling or microRNA processing.
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